The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 Å resolution

Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):114-20. doi: 10.1107/S2053230X14027307. Epub 2015 Jan 1.

Abstract

The enzymatic degradation of plant cell-wall cellulose is central to many industrial processes, including second-generation biofuel production. Key players in this deconstruction are the fungal cellobiohydrolases (CBHs), notably those from family GH7 of the carbohydrate-active enzymes (CAZY) database, which are generally known as CBHI enzymes. Here, three-dimensional structures are reported of the Aspergillus fumigatus CBHI Cel7A solved in uncomplexed and disaccharide-bound forms at resolutions of 1.8 and 1.5 Å, respectively. The product complex with a disaccharide in the +1 and +2 subsites adds to the growing three-dimensional insight into this family of industrially relevant biocatalysts.

Keywords: biofuels; carbohydrate-active enzyme; cellulase; thermal stability.

MeSH terms

  • Aspergillus fumigatus / enzymology*
  • Catalytic Domain
  • Cellobiose / chemistry
  • Cellulose / chemistry
  • Cellulose 1,4-beta-Cellobiosidase / chemistry*
  • Crystallography, X-Ray
  • Enzyme Stability
  • Fungal Proteins / chemistry*
  • Hydrogen Bonding
  • Kinetics
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Secondary

Substances

  • Fungal Proteins
  • Cellobiose
  • Cellulose
  • Cellulose 1,4-beta-Cellobiosidase

Associated data

  • PDB/4V1Z
  • PDB/4V20